Enhanced cutinase - catalyzed hydrolysis of polyethylene terephthalate 1 by covalent fusion to hydrophobins 2 3
نویسندگان
چکیده
1Austrian Centre of Industrial Biotechnology ACIB, 8010 Graz, Austria 8 2 Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, 9 Vienna, 3430 Tulln, Austria 10 3 Microbiology Group, Research Area Biotechnology and Microbiology, Institute of Chemical 11 Engineering, Vienna University of Technology, 1060 Vienna, Austria. 12 4 Institute of Biotechnology, University of Natural Resources and Life Sciences, Vienna, 1190 13 Vienna, Austria 14 5 Institute of Physics and Material Sciences, University of Natural Resources and Life Sciences, 15 Vienna, 1190 Vienna, Austria 16 6 Institute for Inorganic Chemistry, University of Technology Graz, 8010 Graz, Austria 17 7 Institute of Chemical Technologies and Analytics, Vienna University of Technology, Vienna, 18 Austria 19 20
منابع مشابه
Enhanced cutinase-catalyzed hydrolysis of polyethylene terephthalate by covalent fusion to hydrophobins.
Cutinases have shown potential for hydrolysis of the recalcitrant synthetic polymer polyethylene terephthalate (PET). We have shown previously that the rate of this hydrolysis can be enhanced by the addition of hydrophobins, small fungal proteins that can alter the physicochemical properties of surfaces. Here we have investigated whether the PET-hydrolyzing activity of a bacterial cutinase from...
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A lipase from Thermomyces lanuginosus and cutinases from Thermobifida fusca and Fusarium solani hydrolysed poly(ethylene terephthalate) (PET) fabrics and films and bis(benzoyloxyethyl) terephthalate (3PET) endo-wise as shown by MALDI-Tof-MS, LC-UVD/MS, cationic dyeing and XPS analysis. Due to interfacial activation of the lipase in the presence of Triton X-100, a seven-fold increase of hydrolys...
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Cutinases are polyester hydrolases that show a remarkable capability to hydrolyze polyethylene terephthalate (PET) to its monomeric units. This revelation has stimulated research aimed at developing sustainable and green cutinase-catalyzed PET recycling methods. Leaf and branch compost cutinase (LCC) is particularly suited toward these ends given its relatively high PET hydrolysis activity and ...
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This study unambiguously confirms hydrolysis using cutinase of the persistent synthetic polymer poly(ethylene terephthalate), the most important synthetic fiber in the textile industry by direct measurement and identification of the different hydrolysis products. In this aqueous heterogeneous system, dissolved cutinase from Fusarium solani pisi acts on different solid poly(ethylene terephthalat...
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